Evidence map›Paper›PMID 31624254›Full record

ArticleNature communications2019

Transforming protein-polymer conjugate purification by tuning protein solubility.

Stefanie L Baker, Aravinda Munasinghe, Bibifatima Kaupbayeva, Nin Rebecca Kang, Marie Certiat, Hironobu Murata, Krzysztof Matyjaszewski, Ping Lin, Coray M Colina, Alan J Russell

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Stefanie L BakerDepartment of Biomedical Engineering, Scott Hall 4N201, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Aravinda MunasingheDepartment of Chemistry, 354 Leigh Hall, University of Florida, Gainesville, FL, 32611, USA.
Bibifatima KaupbayevaCenter for Polymer-Based Protein Engineering, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Nin Rebecca KangDepartment of Biomedical Engineering, Scott Hall 4N201, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.ORCID http://orcid.org/0000-0001-7606-1991
Marie CertiatDepartment of Chemistry, 354 Leigh Hall, University of Florida, Gainesville, FL, 32611, USA.
Hironobu MurataCenter for Polymer-Based Protein Engineering, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Krzysztof MatyjaszewskiCenter for Polymer-Based Protein Engineering, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.ORCID http://orcid.org/0000-0003-1960-3402
Ping LinDepartment of Chemistry, 354 Leigh Hall, University of Florida, Gainesville, FL, 32611, USA.ORCID http://orcid.org/0000-0002-6141-5424
Coray M ColinaDepartment of Chemistry, 354 Leigh Hall, University of Florida, Gainesville, FL, 32611, USA.ORCID https://orcid.org/0000-0003-2367-1352
Alan J RussellDepartment of Biomedical Engineering, Scott Hall 4N201, Carnegie Mellon University, Pittsburgh, PA, 15213, USA. alanrussell@cmu.edu.ORCID http://orcid.org/0000-0001-5101-4371

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Almost all commercial proteins are purified using ammonium sulfate precipitation. Protein-polymer conjugates are synthesized from pure starting materials, and the struggle to separate conjugates from polymer, native protein, and from isomers has vexed scientists for decades. We have discovered that covalent polymer attachment has a transformational effect on protein solubility in salt solutions. Here, protein-polymer conjugates with a variety of polymers, grafting densities, and polymer lengths are generated using atom transfer radical polymerization. Charged polymers increase conjugate solubility in ammonium sulfate and completely prevent precipitation even at 100% saturation. Atomistic molecular dynamic simulations show the impact is driven by an anti-polyelectrolyte effect from zwitterionic polymers. Uncharged polymers exhibit polymer length-dependent decreased solubility. The differences in salting-out are then used to simply purify mixtures of conjugates and native proteins into single species. Increasing protein solubility in salt solutions through polymer conjugation could lead to many new applications of protein-polymer conjugates.

Indexed as

PolymerizationSolubilityElectrophoresis, Polyacrylamide GelPolymersProtein ConformationProteinsSaltsSolutionsPolymersProteinsSaltsSolutions

Identifiers

PMID31624254
PMCPMC6797786

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.